ID   BGLS_RUMAL              Reviewed;         947 AA.
AC   P15885;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Beta-glucosidase;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
OS   Ruminococcus albus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F-40;
RX   PubMed=2106673; DOI=10.1093/nar/18.3.671;
RA   Ohmiya K., Takano M., Shimizu S.;
RT   "DNA sequence of a beta-glucosidase from Ruminococcus albus.";
RL   Nucleic Acids Res. 18:671-671(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; X15415; CAA33461.1; -; Genomic_DNA.
DR   PIR; S08243; S08243.
DR   AlphaFoldDB; P15885; -.
DR   SMR; P15885; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   eggNOG; COG1472; Bacteria.
DR   UniPathway; UPA00696; -.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..947
FT                   /note="Beta-glucosidase"
FT                   /id="PRO_0000210779"
FT   ACT_SITE        696
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   947 AA;  104278 MW;  C43B8CDD9D60A115 CRC64;
     MIKLDWNEYL EKAAEVNAEG AVLLVNNGVL PLDKNAVTQV FGRIQLDYYK SGTGSGGMVN
     VAKVTGITDG LIEAGAKLNE DVLKAYKDYV AEHPYDYGEG WGGEPWCQEE MPLDDSLVKR
     AAESSDTAIC IIGRTAGEEQ DNSCKAGSYL LTDGEKAILR KVRDNFSKMV ILLNVGNIID
     MGFIDEFSPD AVMYVWQGGM TGGTGTARVL LGEVSPCGKL PDTIAYDITD YPSDKNFHNR
     DVDIYAEDIF VGYRYFDTFA KDRVRFPFGY GLSYTQFEIS AEGRKTDDGV VITAKVKNIG
     SAAGKEVVQV YLEAPNCKLG KAARVLCGFE KTKVLAPNEE QTLTIEVTER DIASYDDSGI
     TGNAFAWVEE AGEYTFYAGS DVRSAKECFA FTLDSTKVIE QLEQALAPVT PFKRMVRTAE
     GLSYEDTPLS KVDEAARRLG YLPAETAYTG DKGIALSDVA HGKNTLDEFI AQLDDNDLNC
     LVRGEGMCSP KVTPGTAAAF GGVAKHLEEL GIPAGCCSDG PSGMRLDVGT KAFSLPNGTL
     IAATFNKSLI TELFTYLGLE MRANKVDCLL GPGMNIHRHP LNGRNFEYFS EDPFLTGTMA
     AAELEGLHSV GVEGTIKHFC ANNQETNRHF IDSVASERAL REIYLKGFEI AVRKSKARSV
     MTTYGKVNGL WTAGSFDLNT MILRKQWGFD GFTMTDWWAN INDRGCAPDK NNFAAMVRAQ
     NDVYMVCADG ESGSDNVIAA LADGRLTRAE LQRSARNILS FMMSTHAMAR KLGEDEAVEV
     INKPAETVDD GEGDRVFLLD GDLTIDMSGV KTERNLDYSF TVDVAQFGQY RMEMTASSTQ
     SELAQMPVTV FSMGTAWGTF TWNGTGGKPV TFAVEEMPMF SRYTIFRLHF GLGGLDMDKI
     VFKKIRPAEA QVCRLRISER WLQTQTYFWL KANFQSKKLL RGRRAYR
//